Sato H, Weisel J W
Department of Polymer Chemistry, Kyoto University, Japan.
Thromb Res. 1990 May 1;58(3):205-12. doi: 10.1016/0049-3848(90)90090-y.
Polymerization of purified fragment X preparations, obtained from a late stage 2 plasmin digest of fibrinogen, was studied by turbidimetry and electron microscopy. The thrombin-induced polymerization of fragment X caused a rapid increase in turbidity followed by a slow decrease. The initial turbidity increase of fragment X polymers was considerably greater than that of normal fibrin. Electron microscopy carried out at different time points in the reaction revealed that initially there was a great deal of lateral aggregation of fragment X fibers. At later times, electron microscopy showed that there was more dispersal or disruption of the fibers, corresponding to the decrease in turbidity. The slow decrease in turbidity was apparently caused by the rearrangement and/or splitting apart of fragment X fibers, starting from a state similar to a very coarse clot, with much aggregation of fibers, to a delicate meshwork, similar to a fine clot. These changes in clot and fiber structure may result from cleavages partly in the carboxy-terminal region of the gamma chains and the amino-terminal region of the B beta chain of fragment X or the influence of other non-clottable fragments present in these preparations.
通过比浊法和电子显微镜研究了从纤维蛋白原的晚期2型纤溶酶消化物中获得的纯化片段X制剂的聚合情况。凝血酶诱导的片段X聚合导致浊度迅速增加，随后缓慢下降。片段X聚合物的初始浊度增加明显大于正常纤维蛋白。在反应的不同时间点进行的电子显微镜观察显示，最初片段X纤维有大量横向聚集。在后期，电子显微镜显示纤维有更多的分散或破坏，这与浊度的降低相对应。浊度的缓慢下降显然是由片段X纤维的重排和/或分裂引起的，从类似于非常粗糙凝块的状态开始，纤维大量聚集，到类似于精细凝块的精致网状结构。凝块和纤维结构的这些变化可能是由于片段X的γ链羧基末端区域和Bβ链氨基末端区域的部分切割，或这些制剂中存在的其他不可凝片段的影响。
